The Molecular Modeling Section uses and develops theoretical tools with which to study the forces that govern the structure and interaction of globular protein molecules, to study and predict the three-dimensional structure of these molecules, and to engineer protein molecules with improved properties. In the past year, we (1) tested a new fast way of computing the hydrophobic force by using it in a protein folding study in which the structures of two small protein molecules were successfully predicted, (2) worked on discovering the sequence-structural motif correlation for the alpha- beta loops of alpha/beta barrel proteins, (3) found one-to-one correspondence between the beta-barrel residues that constitute the VL-VH interface of antibody Fv and the central beta-barrel residues in the alpha/beta barrel proteins, (4) discovered that uteroglobin has a structural motif similar to a fragment of colicin A that is supposed to lie flat on the surface of the membrane, (5) designed modifications to "humanize" the mouse mAb B3, and (6) suggested modifications to the translocation domain of Pseudomonas exotoxin (PE) so that the specificity of its cleavage site at 279-280 is changed from that for furin to that for matrix metalloproteinase and to urokinase-like serine protease.